NMDE1_RAT
ID NMDE1_RAT Reviewed; 1464 AA.
AC Q00959; O08948; Q63728;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 2A;
DE Short=GluN2A {ECO:0000303|PubMed:27618671};
DE AltName: Full=Glutamate [NMDA] receptor subunit epsilon-1;
DE AltName: Full=N-methyl D-aspartate receptor subtype 2A;
DE Short=NMDAR2A {ECO:0000303|PubMed:8428958};
DE Short=NR2A {ECO:0000303|PubMed:1350383, ECO:0000303|PubMed:9509416};
DE Flags: Precursor;
GN Name=Grin2a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1350383; DOI=10.1126/science.256.5060.1217;
RA Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
RA Burnashev N., Sakmann B., Seeburg P.H.;
RT "Heteromeric NMDA receptors: molecular and functional distinction of
RT subtypes.";
RL Science 256:1217-1221(1992).
RN [2]
RP SEQUENCE REVISION TO 595 AND 597-598.
RA Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
RA Burnashev N., Sakmann B., Seeburg P.H.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Forebrain;
RX PubMed=8428958; DOI=10.1016/s0021-9258(18)53849-7;
RA Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H., Yokoi M.,
RA Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.;
RT "Molecular characterization of the family of the N-methyl-D-aspartate
RT receptor subunits.";
RL J. Biol. Chem. 268:2836-2843(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Boulter J.;
RT "Nucleotide sequence of rat NMDA receptor gene NMDAR2A.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH DLG4.
RX PubMed=7569905; DOI=10.1126/science.7569905;
RA Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.;
RT "Domain interaction between NMDA receptor subunits and the postsynaptic
RT density protein PSD-95.";
RL Science 269:1737-1740(1995).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9509416;
RA Jin D.H., Jung Y.W., Ko B.H., Moon I.S.;
RT "Immunoblot analyses on the differential distribution of NR2A and NR2B
RT subunits in the adult rat brain.";
RL Mol. Cells 7:749-754(1997).
RN [7]
RP INTERACTION WITH AIP1.
RX PubMed=9694864; DOI=10.1074/jbc.273.33.21105;
RA Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M.,
RA Toyoda A., Suedhof T.C., Takai Y.;
RT "A novel multiple PDZ domain-containing molecule interacting with N-methyl-
RT d-aspartate receptors and neuronal cell adhesion proteins.";
RL J. Biol. Chem. 273:21105-21110(1998).
RN [8]
RP INTERACTION WITH PATJ.
RX PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT neuroligins.";
RL Mol. Cell. Neurosci. 11:161-172(1998).
RN [9]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN1 AND
RP GRIN3A.
RX PubMed=11160393; DOI=10.1523/jneurosci.21-04-01228.2001;
RA Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S.,
RA Sucher N.J., Heinemann S.F.;
RT "Assembly with the NR1 subunit is required for surface expression of NR3A-
RT containing NMDA receptors.";
RL J. Neurosci. 21:1228-1237(2001).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN3A AND PPP2CB.
RX PubMed=11588171; DOI=10.1523/jneurosci.21-20-07985.2001;
RA Chan S.F., Sucher N.J.;
RT "An NMDA receptor signaling complex with protein phosphatase 2A.";
RL J. Neurosci. 21:7985-7992(2001).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
RX PubMed=12391275; DOI=10.1124/mol.62.5.1119;
RA Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.;
RT "Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2
RT subunits.";
RL Mol. Pharmacol. 62:1119-1127(2002).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
RX PubMed=11929923; DOI=10.1152/jn.00531.2001;
RA Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V.,
RA Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J.,
RA Lipton S.A.;
RT "Characterization and comparison of the NR3A subunit of the NMDA receptor
RT in recombinant systems and primary cortical neurons.";
RL J. Neurophysiol. 87:2052-2063(2002).
RN [13]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN1 AND
RP GRIN3B.
RX PubMed=14602821; DOI=10.1523/jneurosci.23-31-10064.2003;
RA Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
RT "Specific assembly with the NMDA receptor 3B subunit controls surface
RT expression and calcium permeability of NMDA receptors.";
RL J. Neurosci. 23:10064-10073(2003).
RN [14]
RP INTERACTION WITH LRFN2.
RX PubMed=16495444; DOI=10.1523/jneurosci.3799-05.2006;
RA Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.;
RT "A novel family of adhesion-like molecules that interacts with the NMDA
RT receptor.";
RL J. Neurosci. 26:2174-2183(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929;
RP SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [16]
RP FUNCTION, INTERACTION WITH RPH3A AND DLG4, AND SUBCELLULAR LOCATION.
RX PubMed=26679993; DOI=10.1038/ncomms10181;
RA Stanic J., Carta M., Eberini I., Pelucchi S., Marcello E., Genazzani A.A.,
RA Racca C., Mulle C., Di Luca M., Gardoni F.;
RT "Rabphilin 3A retains NMDA receptors at synaptic sites through interaction
RT with GluN2A/PSD-95 complex.";
RL Nat. Commun. 6:10181-10181(2015).
RN [17]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22960932; DOI=10.1038/nn.3214;
RA Rodenas-Ruano A., Chavez A.E., Cossio M.J., Castillo P.E., Zukin R.S.;
RT "REST-dependent epigenetic remodeling promotes the developmental switch in
RT synaptic NMDA receptors.";
RL Nat. Neurosci. 15:1382-1390(2012).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=28384476; DOI=10.1016/j.neuron.2017.03.018;
RA Sun W., Hansen K.B., Jahr C.E.;
RT "Allosteric Interactions between NMDA Receptor Subunits Shape the
RT Developmental Shift in Channel Properties.";
RL Neuron 94:58-64(2017).
RN [19]
RP INTERACTION WITH ARC.
RX PubMed=31080121; DOI=10.1016/j.str.2019.04.001;
RA Nielsen L.D., Pedersen C.P., Erlendsson S., Teilum K.;
RT "The capsid domain of Arc changes its oligomerization propensity through
RT direct interaction with the NMDA receptor.";
RL Structure 0:0-0(2019).
RN [20] {ECO:0007744|PDB:2A5S, ECO:0007744|PDB:2A5T}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 402-539 AND 661-802 IN COMPLEXES
RP WITH GRIN1 AND GLUTAMATE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN,
RP AND DISULFIDE BOND.
RX PubMed=16281028; DOI=10.1038/nature04089;
RA Furukawa H., Singh S.K., Mancusso R., Gouaux E.;
RT "Subunit arrangement and function in NMDA receptors.";
RL Nature 438:185-192(2005).
RN [21] {ECO:0007744|PDB:4JWX}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 402-539 AND 661-802 IN COMPLEX
RP WITH SYNTHETIC AGONIST, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=23625947; DOI=10.1124/mol.113.085803;
RA Hansen K.B., Tajima N., Risgaard R., Perszyk R.E., Jorgensen L.,
RA Vance K.M., Ogden K.K., Clausen R.P., Furukawa H., Traynelis S.F.;
RT "Structural determinants of agonist efficacy at the glutamate binding site
RT of N-methyl-D-aspartate receptors.";
RL Mol. Pharmacol. 84:114-127(2013).
RN [22] {ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF5, ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 402-539 AND 661-802 IN COMPLEXES
RP WITH GRIN1 AND GLUTAMATE, FUNCTION, SUBUNIT, DISULFIDE BONDS, AND
RP MUTAGENESIS OF PHE-416; TYR-730 AND VAL-734.
RX PubMed=24462099; DOI=10.1016/j.neuron.2013.11.033;
RA Jespersen A., Tajima N., Fernandez-Cuervo G., Garnier-Amblard E.C.,
RA Furukawa H.;
RT "Structural insights into competitive antagonism in NMDA receptors.";
RL Neuron 81:366-378(2014).
RN [23] {ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57, ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59, ECO:0007744|PDB:5JTY}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 402-539 AND 661-800 IN COMPLEX
RP WITH GRIN1 AND GLUTAMATE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISULFIDE BONDS.
RX PubMed=27618671; DOI=10.1016/j.neuron.2016.08.014;
RA Yi F., Mou T.C., Dorsett K.N., Volkmann R.A., Menniti F.S., Sprang S.R.,
RA Hansen K.B.;
RT "Structural Basis for Negative Allosteric Modulation of GluN2A-Containing
RT NMDA Receptors.";
RL Neuron 91:1316-1329(2016).
RN [24] {ECO:0007744|PDB:5TPW, ECO:0007744|PDB:5TQ0, ECO:0007744|PDB:5TQ2}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 34-393 IN COMPLEX WITH GRIN1 AND
RP ZINC, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT,
RP MUTAGENESIS OF LYS-233; ASN-264 AND ASP-282, AND DISULFIDE BONDS.
RX PubMed=27916457; DOI=10.1016/j.neuron.2016.11.006;
RA Romero-Hernandez A., Simorowski N., Karakas E., Furukawa H.;
RT "Molecular Basis for Subtype Specificity and High-Affinity Zinc Inhibition
RT in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain.";
RL Neuron 92:1324-1336(2016).
RN [25] {ECO:0007744|PDB:5U8C}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 402-539 AND 661-802 IN COMPLEX
RP WITH GRIN1 AND SYNTHETIC ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=28468946; DOI=10.1124/mol.116.107912;
RA Romero-Hernandez A., Furukawa H.;
RT "Novel Mode of Antagonist Binding in NMDA Receptors Revealed by the Crystal
RT Structure of the GluN1-GluN2A Ligand-Binding Domain Complexed to NVP-
RT AAM077.";
RL Mol. Pharmacol. 92:22-29(2017).
RN [26] {ECO:0007744|PDB:5DEX, ECO:0007744|PDB:5VIH, ECO:0007744|PDB:5VIJ}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 402-539 AND 566-800 IN COMPLEX
RP WITH GRIN1, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=28760974; DOI=10.1073/pnas.1707752114;
RA Lind G.E., Mou T.C., Tamborini L., Pomper M.G., De Micheli C., Conti P.,
RA Pinto A., Hansen K.B.;
RT "Structural basis of subunit selectivity for competitive NMDA receptor
RT antagonists with preference for GluN2A over GluN2B subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E6942-E6951(2017).
RN [27] {ECO:0007744|PDB:5VII}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 402-539 AND 566-800 IN COMPLEX
RP WITH GRIN1, SUBUNIT, AND DISULFIDE BONDS.
RA Mou T.C., Sprang S.R., Hansen K.B.;
RT "Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains
RT with glycine and antagonist, phenyl-ACEPC.";
RL Submitted (APR-2017) to the PDB data bank.
CC -!- FUNCTION: Component of NMDA receptor complexes that function as
CC heterotetrameric, ligand-gated ion channels with high calcium
CC permeability and voltage-dependent sensitivity to magnesium. Channel
CC activation requires binding of the neurotransmitter glutamate to the
CC epsilon subunit, glycine binding to the zeta subunit, plus membrane
CC depolarization to eliminate channel inhibition by Mg(2+). Sensitivity
CC to glutamate and channel kinetics depend on the subunit composition;
CC channels containing GRIN1 and GRIN2A have lower sensitivity to
CC glutamate and faster deactivation kinetics than channels formed by
CC GRIN1 and GRIN2B (PubMed:28384476). Contributes to the slow phase of
CC excitatory postsynaptic current, long-term synaptic potentiation, and
CC learning (By similarity). {ECO:0000250|UniProtKB:P35436,
CC ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:16281028,
CC ECO:0000269|PubMed:23625947, ECO:0000269|PubMed:24462099,
CC ECO:0000269|PubMed:26679993, ECO:0000269|PubMed:27618671,
CC ECO:0000269|PubMed:27916457, ECO:0000269|PubMed:28384476,
CC ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:28760974,
CC ECO:0000269|PubMed:8428958}.
CC -!- ACTIVITY REGULATION: Channel activity is inhibited by nM concentrations
CC of Zn(2+). {ECO:0000269|PubMed:27916457}.
CC -!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of
CC two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B,
CC GRIN2C or GRIN2D) (in vitro) (PubMed:1350383, PubMed:8428958,
CC PubMed:28384476, PubMed:16281028, PubMed:23625947, PubMed:24462099,
CC PubMed:27618671, PubMed:27916457, PubMed:28468946, PubMed:28760974,
CC Ref.27). Can also form heterotetrameric channels that contain at least
CC one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or
CC GRIN3B (PubMed:11160393, PubMed:11588171, PubMed:12391275,
CC PubMed:11929923). In vivo, the subunit composition may depend on the
CC expression levels of the different subunits (Probable). Found in a
CC complex with GRIN1, GRIN3A and PPP2CB (PubMed:11588171). Found in a
CC complex with GRIN1 and GRIN3B (PubMed:14602821). Interacts with AIP1
CC (PubMed:9694864). Interacts with HIP1 and NETO1. Interacts with SNX27
CC (via PDZ domain); the interaction is required for recycling to the
CC plasma membrane when endocytosed and prevent degradation in lysosomes
CC (By similarity). Interacts with PDZ domains of PATJ and DLG4
CC (PubMed:7569905, PubMed:9647694). Interacts with LRFN2
CC (PubMed:16495444). Interacts with RPH3A and DLG4; this ternary complex
CC regulates NMDA receptor composition at postsynaptic membranes
CC (PubMed:26679993). Interacts with SORCS2 (By similarity). Interacts
CC with ARC; preventing ARC oligomerization (PubMed:31080121).
CC {ECO:0000250|UniProtKB:P35436, ECO:0000269|PubMed:11160393,
CC ECO:0000269|PubMed:11588171, ECO:0000269|PubMed:11929923,
CC ECO:0000269|PubMed:12391275, ECO:0000269|PubMed:1350383,
CC ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:16281028,
CC ECO:0000269|PubMed:16495444, ECO:0000269|PubMed:23625947,
CC ECO:0000269|PubMed:24462099, ECO:0000269|PubMed:26679993,
CC ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:27916457,
CC ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946,
CC ECO:0000269|PubMed:28760974, ECO:0000269|PubMed:31080121,
CC ECO:0000269|PubMed:7569905, ECO:0000269|PubMed:8428958,
CC ECO:0000269|PubMed:9647694, ECO:0000269|PubMed:9694864,
CC ECO:0000269|Ref.27, ECO:0000305}.
CC -!- INTERACTION:
CC Q00959; P31016: Dlg4; NbExp=5; IntAct=EBI-630970, EBI-375655;
CC Q00959; Q8R4I7: Neto1; Xeno; NbExp=4; IntAct=EBI-630970, EBI-2314926;
CC Q00959; P05480: Src; Xeno; NbExp=4; IntAct=EBI-630970, EBI-298680;
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000269|PubMed:26679993}. Cell membrane
CC {ECO:0000269|PubMed:11160393, ECO:0000269|PubMed:1350383,
CC ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:16281028,
CC ECO:0000269|PubMed:23625947, ECO:0000269|PubMed:24462099,
CC ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:27916457,
CC ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946,
CC ECO:0000269|PubMed:28760974, ECO:0000269|PubMed:8428958}; Multi-pass
CC membrane protein {ECO:0000305}. Synapse {ECO:0000250|UniProtKB:P35436}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:26679993,
CC ECO:0000269|PubMed:9509416}; Multi-pass membrane protein {ECO:0000305}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P35436}.
CC Note=Expression at the dendrite cell membrane and at synapses is
CC regulated by SORCS2 and the retromer complex.
CC {ECO:0000250|UniProtKB:P35436}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, olfactory bulb,
CC hippocampus including the dentate gyrus, striatum, thalamus, superior
CC colliculus, inferior colliculus, midbrain and cerebellum (at protein
CC level) (PubMed:22960932, PubMed:9509416). Detected in brain cortex,
CC hypothalamus and cerebellum (PubMed:1350383).
CC {ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:22960932,
CC ECO:0000269|PubMed:9509416}.
CC -!- DEVELOPMENTAL STAGE: Expressed during postnatal days P3 to P60, with
CC increased expression after postnatal day 3.
CC {ECO:0000269|PubMed:22960932}.
CC -!- DOMAIN: Contains an N-terminal domain, a ligand-binding domain and a
CC transmembrane domain. Agonist binding to the extracellular ligand-
CC binding domains triggers channel gating. {ECO:0000305|PubMed:16281028}.
CC -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC transmembrane span does not cross the membrane, but is part of a
CC discontinuously helical region that dips into the membrane and is
CC probably part of the pore and of the selectivity filter.
CC {ECO:0000250|UniProtKB:B7ZSK1}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR2A/GRIN2A subfamily. {ECO:0000305}.
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DR EMBL; M91561; AAC03565.1; -; mRNA.
DR EMBL; D13211; BAA02498.1; -; mRNA.
DR EMBL; AF001423; AAB58801.1; -; mRNA.
DR PIR; A43274; A43274.
DR RefSeq; NP_036705.3; NM_012573.3.
DR PDB; 2A5S; X-ray; 1.70 A; A=401-539.
DR PDB; 2A5T; X-ray; 2.00 A; B=401-539.
DR PDB; 4JWX; X-ray; 1.50 A; A=404-539, A=661-802.
DR PDB; 4NF4; X-ray; 2.00 A; B=402-539, B=661-802.
DR PDB; 4NF5; X-ray; 1.90 A; B=402-539, B=661-802.
DR PDB; 4NF6; X-ray; 2.10 A; B=402-539, B=661-802.
DR PDB; 4NF8; X-ray; 1.86 A; B=402-539, B=661-802.
DR PDB; 5DEX; X-ray; 2.40 A; B=402-539, B=661-802.
DR PDB; 5I56; X-ray; 2.28 A; B=402-539, B=661-800.
DR PDB; 5I57; X-ray; 1.70 A; B=402-539, B=661-800.
DR PDB; 5I58; X-ray; 2.52 A; B=402-539, B=661-800.
DR PDB; 5I59; X-ray; 2.25 A; B=402-539, B=661-800.
DR PDB; 5JTY; X-ray; 2.72 A; B=402-539, B=661-800.
DR PDB; 5TPW; X-ray; 2.91 A; B=34-393.
DR PDB; 5TQ0; X-ray; 2.70 A; B=34-393.
DR PDB; 5TQ2; X-ray; 3.29 A; B=34-393.
DR PDB; 5U8C; X-ray; 1.60 A; B=402-539, A=661-802.
DR PDB; 5VIH; X-ray; 2.40 A; B=402-539, B=566-800.
DR PDB; 5VII; X-ray; 1.95 A; B=402-539, B=566-800.
DR PDB; 5VIJ; X-ray; 2.10 A; B=402-539, B=566-800.
DR PDB; 6MM9; EM; 5.97 A; B/D=1-837.
DR PDB; 6MMA; EM; 6.31 A; B/D=1-837.
DR PDB; 6MMB; EM; 12.70 A; B/D=1-837.
DR PDB; 6MMG; EM; 6.23 A; B/D=1-837.
DR PDB; 6MMH; EM; 8.21 A; B/D=1-837.
DR PDB; 6MMI; EM; 8.93 A; B/D=1-837.
DR PDB; 6MMJ; EM; 16.50 A; B/D=1-837.
DR PDB; 6MMK; EM; 6.08 A; B/D=1-837.
DR PDB; 6MML; EM; 7.14 A; B/D=1-837.
DR PDB; 6MMM; EM; 6.84 A; B/D=1-837.
DR PDB; 6MMN; EM; 7.51 A; B/D=1-837.
DR PDB; 6MMP; EM; 6.88 A; B/D=1-837.
DR PDB; 6MMR; EM; 5.13 A; B/D=1-837.
DR PDB; 6MMS; EM; 5.38 A; B/D=1-837.
DR PDB; 6MMT; EM; 7.46 A; B/D=1-837.
DR PDB; 6MMU; EM; 5.30 A; B/D=1-837.
DR PDB; 6MMV; EM; 4.71 A; B/D=1-800.
DR PDB; 6MMW; EM; 6.20 A; B/D=1-837.
DR PDB; 6MMX; EM; 6.99 A; B/D=1-837.
DR PDB; 6ODL; X-ray; 2.30 A; A/B=404-539, A/B=661-801.
DR PDB; 6OVD; X-ray; 2.10 A; B=402-539, B=661-802.
DR PDB; 6OVE; X-ray; 2.00 A; B=402-539, B=568-801.
DR PDB; 6USU; X-ray; 2.09 A; B=402-539, B=661-802.
DR PDB; 6USV; X-ray; 2.30 A; B=402-539, B=661-802.
DR PDB; 6UZ6; X-ray; 1.66 A; B=402-539, B=661-800.
DR PDB; 6UZG; X-ray; 1.94 A; B=402-539, B=661-802.
DR PDB; 6UZR; X-ray; 1.87 A; B=402-539, B=661-802.
DR PDB; 6UZW; X-ray; 2.13 A; B=402-539, B=661-802.
DR PDB; 6UZX; X-ray; 2.41 A; B=402-539, B=661-802.
DR PDBsum; 2A5S; -.
DR PDBsum; 2A5T; -.
DR PDBsum; 4JWX; -.
DR PDBsum; 4NF4; -.
DR PDBsum; 4NF5; -.
DR PDBsum; 4NF6; -.
DR PDBsum; 4NF8; -.
DR PDBsum; 5DEX; -.
DR PDBsum; 5I56; -.
DR PDBsum; 5I57; -.
DR PDBsum; 5I58; -.
DR PDBsum; 5I59; -.
DR PDBsum; 5JTY; -.
DR PDBsum; 5TPW; -.
DR PDBsum; 5TQ0; -.
DR PDBsum; 5TQ2; -.
DR PDBsum; 5U8C; -.
DR PDBsum; 5VIH; -.
DR PDBsum; 5VII; -.
DR PDBsum; 5VIJ; -.
DR PDBsum; 6MM9; -.
DR PDBsum; 6MMA; -.
DR PDBsum; 6MMB; -.
DR PDBsum; 6MMG; -.
DR PDBsum; 6MMH; -.
DR PDBsum; 6MMI; -.
DR PDBsum; 6MMJ; -.
DR PDBsum; 6MMK; -.
DR PDBsum; 6MML; -.
DR PDBsum; 6MMM; -.
DR PDBsum; 6MMN; -.
DR PDBsum; 6MMP; -.
DR PDBsum; 6MMR; -.
DR PDBsum; 6MMS; -.
DR PDBsum; 6MMT; -.
DR PDBsum; 6MMU; -.
DR PDBsum; 6MMV; -.
DR PDBsum; 6MMW; -.
DR PDBsum; 6MMX; -.
DR PDBsum; 6ODL; -.
DR PDBsum; 6OVD; -.
DR PDBsum; 6OVE; -.
DR PDBsum; 6USU; -.
DR PDBsum; 6USV; -.
DR PDBsum; 6UZ6; -.
DR PDBsum; 6UZG; -.
DR PDBsum; 6UZR; -.
DR PDBsum; 6UZW; -.
DR PDBsum; 6UZX; -.
DR AlphaFoldDB; Q00959; -.
DR SMR; Q00959; -.
DR BioGRID; 246574; 19.
DR ComplexPortal; CPX-283; NMDA receptor complex, GluN1-GluN2A.
DR ComplexPortal; CPX-295; NMDA receptor complex, GluN1-GluN2A-GluN2B.
DR CORUM; Q00959; -.
DR DIP; DIP-34031N; -.
DR IntAct; Q00959; 8.
DR MINT; Q00959; -.
DR STRING; 10116.ENSRNOP00000042235; -.
DR BindingDB; Q00959; -.
DR ChEMBL; CHEMBL310; -.
DR DrugCentral; Q00959; -.
DR GuidetoPHARMACOLOGY; 456; -.
DR TCDB; 1.A.10.1.6; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q00959; 7 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q00959; -.
DR PhosphoSitePlus; Q00959; -.
DR SwissPalm; Q00959; -.
DR PaxDb; Q00959; -.
DR PRIDE; Q00959; -.
DR ABCD; Q00959; 2 sequenced antibodies.
DR GeneID; 24409; -.
DR KEGG; rno:24409; -.
DR UCSC; RGD:2737; rat.
DR CTD; 2903; -.
DR RGD; 2737; Grin2a.
DR eggNOG; KOG1053; Eukaryota.
DR InParanoid; Q00959; -.
DR PhylomeDB; Q00959; -.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-RNO-9609736; Assembly and cell surface presentation of NMDA receptors.
DR EvolutionaryTrace; Q00959; -.
DR PRO; PR:Q00959; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR GO; GO:0005261; F:cation channel activity; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR GO; GO:0035254; F:glutamate receptor binding; IPI:RGD.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR GO; GO:0042165; F:neurotransmitter binding; IDA:RGD.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0022843; F:voltage-gated cation channel activity; IMP:RGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0001508; P:action potential; IMP:RGD.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:RGD.
DR GO; GO:0071359; P:cellular response to dsRNA; IEP:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
DR GO; GO:0071286; P:cellular response to magnesium ion; IEP:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
DR GO; GO:0071294; P:cellular response to zinc ion; IMP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
DR GO; GO:0097061; P:dendritic spine organization; IMP:UniProtKB.
DR GO; GO:0033058; P:directional locomotion; ISO:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0040011; P:locomotion; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0007613; P:memory; IDA:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:ComplexPortal.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; ISO:RGD.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IC:ComplexPortal.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:UniProtKB.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0060359; P:response to ammonium ion; IEP:RGD.
DR GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IMP:ARUK-UCL.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0010042; P:response to manganese ion; IEP:RGD.
DR GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0051707; P:response to other organism; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0048511; P:rhythmic process; IDA:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0042428; P:serotonin metabolic process; ISO:RGD.
DR GO; GO:0030431; P:sleep; ISO:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR GO; GO:0001964; P:startle response; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR018884; NMDAR2_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR Pfam; PF10565; NMDAR2_C; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1464
FT /note="Glutamate receptor ionotropic, NMDA 2A"
FT /id="PRO_0000011576"
FT TOPO_DOM 23..555
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 577..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 601..620
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 621..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 626..645
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 646..816
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 838..1464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 599..620
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT REGION 989..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1462..1464
FT /note="PDZ-binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 989..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27916457,
FT ECO:0007744|PDB:5TPW"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27916457,
FT ECO:0007744|PDB:5TPW"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27916457,
FT ECO:0007744|PDB:5TPW"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27916457,
FT ECO:0007744|PDB:5TPW"
FT BINDING 511..513
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0007744|PDB:2A5S, ECO:0007744|PDB:2A5T,
FT ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57,
FT ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59,
FT ECO:0007744|PDB:5JTY"
FT BINDING 518
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:24462099, ECO:0000269|PubMed:27618671,
FT ECO:0007744|PDB:2A5S, ECO:0007744|PDB:2A5T,
FT ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57,
FT ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59,
FT ECO:0007744|PDB:5JTY"
FT BINDING 689..690
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:24462099, ECO:0007744|PDB:2A5S,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4NF4,
FT ECO:0007744|PDB:4NF8"
FT BINDING 730..731
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:24462099, ECO:0007744|PDB:2A5S,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4NF4,
FT ECO:0007744|PDB:4NF8"
FT SITE 614
FT /note="Functional determinant of NMDA receptors"
FT /evidence="ECO:0000250"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..320
FT /evidence="ECO:0000269|PubMed:27916457,
FT ECO:0007744|PDB:5TPW, ECO:0007744|PDB:5TQ0,
FT ECO:0007744|PDB:5TQ2"
FT DISULFID 429..455
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:24462099, ECO:0000269|PubMed:27618671,
FT ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:28760974,
FT ECO:0000269|Ref.27, ECO:0007744|PDB:2A5S,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4JWX,
FT ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:5DEX, ECO:0007744|PDB:5I56,
FT ECO:0007744|PDB:5I57, ECO:0007744|PDB:5I58,
FT ECO:0007744|PDB:5I59, ECO:0007744|PDB:5JTY,
FT ECO:0007744|PDB:5U8C, ECO:0007744|PDB:5VIH,
FT ECO:0007744|PDB:5VII, ECO:0007744|PDB:5VIJ"
FT DISULFID 436..456
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:23625947, ECO:0000269|PubMed:24462099,
FT ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:28468946,
FT ECO:0000269|PubMed:28760974, ECO:0007744|PDB:2A5S,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4JWX,
FT ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:5DEX, ECO:0007744|PDB:5I56,
FT ECO:0007744|PDB:5I57, ECO:0007744|PDB:5I58,
FT ECO:0007744|PDB:5I59, ECO:0007744|PDB:5JTY,
FT ECO:0007744|PDB:5U8C, ECO:0007744|PDB:5VIH,
FT ECO:0007744|PDB:5VII, ECO:0007744|PDB:5VIJ"
FT DISULFID 745..800
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:23625947, ECO:0000269|PubMed:24462099,
FT ECO:0000269|PubMed:28468946, ECO:0007744|PDB:2A5S,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4JWX,
FT ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:5U8C"
FT MUTAGEN 233
FT /note="K->A,R: Nearly abolishes inhibition by Zn(2+)."
FT /evidence="ECO:0000269|PubMed:27916457"
FT MUTAGEN 264
FT /note="N->W: Nearly abolishes inhibition by Zn(2+)."
FT /evidence="ECO:0000269|PubMed:27916457"
FT MUTAGEN 282
FT /note="D->A,H: Nearly abolishes inhibition by Zn(2+)."
FT /evidence="ECO:0000269|PubMed:27916457"
FT MUTAGEN 416
FT /note="F->A: Decreased sensitivity to glutamate."
FT /evidence="ECO:0000269|PubMed:24462099"
FT MUTAGEN 730
FT /note="Y->F,L,M: Strongly decreased sensitivity to
FT glutamate."
FT /evidence="ECO:0000269|PubMed:24462099"
FT MUTAGEN 734
FT /note="V->A: Decreased sensitivity to glutamate."
FT /evidence="ECO:0000269|PubMed:24462099"
FT CONFLICT 246
FT /note="L -> F (in Ref. 3; BAA02498)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="S -> T (in Ref. 3; BAA02498 and 4; AAB58801)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="E -> D (in Ref. 4; AAB58801)"
FT /evidence="ECO:0000305"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5TPW"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:5TQ0"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:5TQ2"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 288..309
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5TQ0"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:5TQ2"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5TQ2"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:5TQ0"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:5TPW"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:5TQ0"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:5TQ0"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:5U8C"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:4JWX"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:4JWX"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 434..447
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 449..458
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 459..471
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:5I58"
FT HELIX 495..501
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 516..519
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 668..671
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:6UZW"
FT HELIX 689..697
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 699..705
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 713..721
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 726..731
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 732..740
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 743..745
FT /evidence="ECO:0007829|PDB:5VII"
FT STRAND 747..751
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:5U8C"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:4JWX"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 772..784
FT /evidence="ECO:0007829|PDB:4JWX"
FT HELIX 787..795
FT /evidence="ECO:0007829|PDB:4JWX"
SQ SEQUENCE 1464 AA; 165469 MW; DC1528E1898DECA4 CRC64;
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE LRNLWGPEQA
TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSQT
FIPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY
RDFISFIKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL
SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF TEEGYQVHPR
LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE
DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV
TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS
NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD
QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTRFNQ RGVEDALVSL
KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFASTG YGIALQKGSP WKRQIDLALL
QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL
FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ GKDSIFGDNM
NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV STESKGNSRP RQLWKKSMES
LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR YLPEEVAHSD ISETSSRATC HREPDNNKNH
KTKDNFKRSM ASKYPKDCSD VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT
LPENVGFPDT YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP
ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR EIDLSRPSRS ISLKDRERLL
EGNLYGSLFS VPSSKLLGNK SSLFPQGLED SKRSKSLLPD HASDNPFLHT YGDDQRLVIG
RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS
TPRVLNSCSN RRVYKKMPSI ESDV
